Skip to main content
SpringerLink
Log in

Glycotope Structures and Intramolecular Affinity Factors of Plant Lectins for Tn/T Antigens

  • Conference paper
  • First Online:
The Molecular Immunology of Complex Carbohydrates-3

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 705))

Abstract

O-glycosylation is a widely distributed posttranslational modification initiated by the addition of GalNAc to serine or threonine residues of polypeptide chains. The GalNAc may be further substituted to form linear/branched sugar chains. Some proteins, like the mucins of vertebrates, are extensively O-glycosylated and consist predominantly of carbohydrate. T antigens, which were originally designated as Thomsen–Friedenreich or TF antigens, are of particular interest in glycobiology since a high expression of the T antigen on the cell surface can be used as a glycomarker [1–3]. Due to the apparent loss of βGalactosyl-transferase, which normally converts the Tn antigen (GalNAcα1-Thr/Ser) into the T antigen (Galβ1,3GalNAcα1-Thr/Ser), the precursor Tn antigen accumulates in cancer cells (Fig. 8.1).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Springer GF (1984) T and Tn, general carcinoma autoantigens. Science 24:1189–1206

    Google Scholar 

  2. Springer GF (1997) Immunoreactive T and Tn epitopes in cancer diagnosis, prognosis, and immunotherapy. J Mol Med 75:594–602

    Article  PubMed  CAS  Google Scholar 

  3. Itzkowitz SH, Bloom EJ, Kokal WA, Modin G, Hakomori SI, Kim YS (1990) Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients. Cancer 66:1960–1966

    Article  PubMed  CAS  Google Scholar 

  4. Springer GF (1995) T and Tn pancarcinoma markers: autoantigenic adhesion molecules in pathogenesis, prebiopsy carcinoma-detection, and long-term breast carcinoma immunotherapy. Crit Rev Oncog 6:57–85

    PubMed  CAS  Google Scholar 

  5. Hakomori SI (1984) Philip Levine award lecture: blood group glycolipid antigens and their modifications as human cancer antigens. Am J Clin Pathol 82:635–648

    PubMed  CAS  Google Scholar 

  6. Hakomori SI (1989) Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens. Adv Cancer Res 52:257–331

    Article  PubMed  CAS  Google Scholar 

  7. Hakomori SI, Wang SM, Young WW (1977) Isoantigenic expression of Forssman glycolipid in human gastric and colonic mucosa: its possible identity with “A-like antigen” in human cancer. Proc Natl Acad Sci USA 74:3023–3027

    Article  PubMed  CAS  Google Scholar 

  8. Taniguchi N, Yokosawa N, Narita M, Mitsuyama T, Makita A (1981) Expression of Forssman antigen synthesis and degradation in human lung cancer. J Natl Cancer Inst 67:577–583

    PubMed  CAS  Google Scholar 

  9. Yoda Y, Ishibashi T, Makita A (1980) Isolation, characterization, and biosynthesis of Forssman antigen in human lung and lung carcinoma. J Biochem 88:1887–1890

    PubMed  CAS  Google Scholar 

  10. Hirohashi S, Clausen H, Yamada T, Shimossato Y, Hakomori SI (1985) Blood group A cross-reacting epitope defined by monoclonal antibodies NCC-LU-35 and -81 expressed in cancer of blood group O or B individuals: its identification as Tn antigen. Proc Natl Acad Sci USA 82:7039–7043

    Article  PubMed  CAS  Google Scholar 

  11. Van Damme EJM, Peumans WJ, Pusztai A, Bardocz S (1997) In: Van Damme EJM, Peumans WJ, Pusztai A, Bardocz S (eds) Handbook of plant lectins: properties and biomedical applications. Wiley, Chichester, pp 64–427

    Google Scholar 

  12. Wu AM, Song SC, Tsai MS, Herp A (2001) A guide to the carbohydrate specificities of applied lectins-2. Adv Exp Med Biol 491:551–585

    PubMed  CAS  Google Scholar 

  13. Rinderle SJ, Goldstein IJ, Matta KL, Ratcliffe RM (1989) Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, that recognizes the T- (or cryptic T)-antigen. J Biol Chem 264:16123–16131

    PubMed  CAS  Google Scholar 

  14. Zenteno E, Lescurain R, Montano LF, Vazquez L, Debray H, Montreuil J (1992) Specificity of Amaranthus leucocarpus lectin. Glycoconj J 9:204–208

    Article  PubMed  CAS  Google Scholar 

  15. Wu AM, Lin SR, Chin LK, Chow LP, Lin JY (1992) Defining the carbohydrate specificities of Abrus precatorius agglutinin as T (Galβ1-3GalNAc) greater than I/II (Galβ1-3/4GlcNAc). J Biol Chem 267:19130–19139

    PubMed  CAS  Google Scholar 

  16. Lotan R, Skutelsky E, Danon D, Sharon N (1975) The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J Biol Chem 250:8518–8523

    PubMed  CAS  Google Scholar 

  17. Wu AM, Wu JH, Chen YY, Song SC, Kabat EA (1999) Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4). Glycobiology 9:1161–1170

    Article  PubMed  CAS  Google Scholar 

  18. Duk M, Lisowska E, Kordowicz M, Waśniowska K (1982) Studies on the specificity of the binding site of Vicia graminea anti-N lectin. Eur J Biochem 123:105–112

    Article  PubMed  CAS  Google Scholar 

  19. Puri K, Gopalakrishnan B, Surolia A (1992) Carbohydrate binding specificity of the Tn-antigen binding lectin from Vicia villosa seeds (VVLB4). FEBS Lett 312:208–212

    Article  PubMed  CAS  Google Scholar 

  20. Wu AM (2004) Polyvalency of Tn (GalNAcalpha1→Ser/Thr) glycotope as a critical factor for Vicia villosa B4 and glycoprotein interactions. FEBS Lett 562:51–58

    Article  PubMed  CAS  Google Scholar 

  21. Singh T, Wu JH, Peumans WJ, Rougé P, Van Damme EJM, Alvarez RA, Blixt O, Wu AM (2006) Carbohydrate specificity of an insecticidal lectin isolated from the leaves of Glechoma hederacea (ground ivy) towards mammalian glycoconjugates. Biochem J 393:331–341

    Article  PubMed  CAS  Google Scholar 

  22. Duk M, Mitra D, Lisowska E, Kabat EA, Sharon N, Lis H (1992) Immunochemical studies on the combining site of the A  +  N blood type specific Moluccella laevis lectin. Carbohydr Res 236:245–258

    Article  PubMed  CAS  Google Scholar 

  23. Piller V, Piller F, Cartron JP (1986) Isolation and characterization of an N-acetylgalactosamine specific lectin from Salvia sclarea seeds. J Biol Chem 261:14069–14075

    PubMed  CAS  Google Scholar 

  24. Wu AM (2005) Lectinochemical studies on the glyco-recognition factors of a Tn (GalNAcalpha1→Ser/Thr) specific lectin isolated from the seeds of Salvia sclarea. J Biomed Sci 12:167–184

    Article  PubMed  CAS  Google Scholar 

  25. Vega N, Perez G (2006) Isolation and characterisation of a Salvia bogotensis seed lectin specific for the Tn antigen. Phytochemistry 67:347–355

    Article  PubMed  CAS  Google Scholar 

  26. Bird GWG, Wingham J (1974) Haemagglutinins from Salvia. Vox Sang 26:163–166

    Article  PubMed  CAS  Google Scholar 

  27. Wu AM, Wu JH, Lin LH, Lin SH, Liu JH (2003) Binding profile of Artocarpus integrifolia agglutinin (Jacalin). Life Sci 72:2285–2302

    Article  PubMed  CAS  Google Scholar 

  28. Singh T, Chatterjee U, Wu JH, Chatterjee BP, Wu AM (2005) Carbohydrate recognition factors of a Talpha (Galbeta1→3GalNAcalpha1→Ser/Thr) and Tn (GalNAcalpha1→Ser/Thr) specific lectin isolated from the seeds of Artocarpus lakoocha. Glycobiology 15:67–78

    Article  PubMed  CAS  Google Scholar 

  29. Sarkar M, Wu AM, Kabat EA (1981) Immunochemical studies on the carbohydrate specificity of Maclura pomifera lectin. Arch Biochem Biophys 209:204–218

    Article  PubMed  CAS  Google Scholar 

  30. Wu AM (2005) Polyvalent GalNAcalpha1→Ser/Thr (Tn) and Galbeta1→3GalNAcalpha1­→Ser/Thr (T alpha) as the most potent recognition factors involved in Maclura pomifera agglutinin-glycan interactions. J Biomed Sci 12:135–152

    Article  PubMed  CAS  Google Scholar 

  31. Singh T, Wu JH, Peumans WJ, Rougé P, Van Damme EJM, Wu AM (2007) Recognition profile of Morus nigra agglutinin (Morniga G) expressed by monomeric ligands, simple clusters and mammalian polyvalent glycotopes. Mol Immunol 44:451–462

    Article  PubMed  CAS  Google Scholar 

  32. Zenteno R, Chavez R, Portugal D, Paez A, Lascurain R, Zenteno E (1995) Purification of a N-acetyl-d-galactosamine specific lectin from the orchid Laelia autumnalis. Phytochemistry 40:651–655

    Article  PubMed  CAS  Google Scholar 

  33. Wang W, Peumans WJ, Rougé P, Rossi C, Proost P, Chen J, Van Damme EJM (2003) Leaves of the Lamiaceae species Glechoma hederacea (ground ivy) contain a lectin that is structurally and evolutionary related to the legume lectins. Plant J 33:293–304

    Article  PubMed  CAS  Google Scholar 

  34. Wu AM, Wu JH, Singh T, Chu KC, Peumans WJ, Rouge P, Van Damme EJ (2004) A novel lectin (Morniga M) from mulberry (Morus nigra) bark recognizes oligomannosyl residues in N-glycans. J Biomed Sci 11:874–885

    PubMed  Google Scholar 

  35. Sankaranarayanan R, Sekar K, Banerjee R, Sharma V, Surolia A, Vijayan M (1996) A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold. Nat Struct Biol 3:596–603

    Article  PubMed  CAS  Google Scholar 

  36. Tollefsen S, Kornfeld R (1983) Isolation and characterization of lectins from Vicia villosa. Two distinct carbohydrate binding activities are present in seed extracts. J Biol Chem 258:5165–5171

    PubMed  CAS  Google Scholar 

  37. Babino A, Tello D, Rojas A, Bay S, Osinaga E, Alzari PM (2003) The crystal structure of a plant lectin in complex with the Tn antigen. FEBS Lett 536:106–110

    Article  PubMed  CAS  Google Scholar 

  38. Kulkarni KA, Sinha S, Katiyar S, Surolia A, Vijayan M, Suguna K (2005) Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: a crystallographic, thermodynamic and modelling study. FEBS Lett 579:6775–6780

    Article  PubMed  CAS  Google Scholar 

  39. Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K (2006) Structural basis for the carbohydrate-specificity of basic winged-bean lectin and its differential affinity for Gal and GalNAc. Acta Crystallogr D Biol Crystallogr D62:1319–1324

    Article  CAS  Google Scholar 

  40. Lee X, Thompson A, Zhiming Z, Ton-That H, Biesterfeldt J, Ogata C, Xu L, Johnston RAZ, Young NM (1998) Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galbeta1, 3GalNAc. J Biol Chem 273:6312–6318

    Article  PubMed  CAS  Google Scholar 

  41. Jeyaprakash AA, Rani PG, Reddy GB, Banumathi S, Betzel C, Surolia A, Vijayan M (2002) Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes. J Mol Biol 321:637–645

    Article  PubMed  CAS  Google Scholar 

  42. Ravishankar R, Ravindran M, Suguna K, Surolia A, Vijayan M (1997) Crystal structure of the peanut lectin-T-antigen complex. Carbohydrate specificity generated by water bridges. Curr Sci 72:855–861

    CAS  Google Scholar 

  43. Transue TR, Smith AK, Mo H, Goldstein IJ, Saper MA (1997) Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin. Nat Struct Biol 4:779–783

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgments

This study was supported by grants from the Chang-Gung Medical Research Project (CMRPD No. 33022), Kwei-san, Tao-yuan, Taiwan, and the National Science Council, Taiwan (NSC 94-2320-B-182-044 and NSC 94-2320-B-182-053).

Author information

Authors and Affiliations

  1. Surfaces Cellulaires et Signalisation chez les Végétaux, UMR UPS-CNRS 5546, Pôle de Biotechnologie végétale, 24 Chemin de Borde Rouge, 31326, Castanet Tolosan, France

    Pierre Rougé

Authors
  1. Pierre Rougé
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Willy J. Peumans
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Els J. M. Van Damme
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Annick Barre
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Tanuja Singh
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. June H. Wu
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Albert M. Wu
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Pierre Rougé .

Editor information

Editors and Affiliations

  1. College of Medicine, Institute of Molecular&Cellular Biology, Chang-Gung University, Kwei-San, Tao-Yuan, 333, Taiwan R.O.C.

    Albert M. Wu

Rights and permissions

Reprints and permissions

Copyright information

© 2011 Springer Science+Business Media, LLC

About this paper

Cite this paper

Rougé, P. et al. (2011). Glycotope Structures and Intramolecular Affinity Factors of Plant Lectins for Tn/T Antigens. In: Wu, A. (eds) The Molecular Immunology of Complex Carbohydrates-3. Advances in Experimental Medicine and Biology, vol 705. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7877-6_8

Download citation

Publish with us

Policies and ethics

Search

Navigation